ID A0A4P8YL57_9ENTR Unreviewed; 813 AA.
AC A0A4P8YL57;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Dimethylsulfoxide reductase subunit A {ECO:0000313|EMBL:QCT20736.1};
DE EC=1.8.5.3 {ECO:0000313|EMBL:QCT20736.1};
GN Name=dmsA {ECO:0000313|EMBL:QCT20736.1};
GN ORFNames=FEM41_14320 {ECO:0000313|EMBL:QCT20736.1};
OS Jejubacter calystegiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Jejubacter.
OX NCBI_TaxID=2579935 {ECO:0000313|EMBL:QCT20736.1, ECO:0000313|Proteomes:UP000302163};
RN [1] {ECO:0000313|EMBL:QCT20736.1, ECO:0000313|Proteomes:UP000302163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSNA2 {ECO:0000313|EMBL:QCT20736.1,
RC ECO:0000313|Proteomes:UP000302163};
RA Jiang L., Jeong J.C., Kim C.Y., Kim D.H., Kim S.W., Lee j.;
RT "Complete genome sequence of Izhakiella calystegiae KSNA2, an endophyte
RT isolated from beach morning glory (Calystegia soldanella).";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP040428; QCT20736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P8YL57; -.
DR KEGG; izh:FEM41_14320; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000302163; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR CDD; cd02794; MopB_CT_DmsA-EC; 1.
DR CDD; cd02770; MopB_DmsA-EC; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 2.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR011888; Anaer_DMSO_reductase.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:QCT20736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000302163};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 55..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 813 AA; 89831 MW; 0B125816942FAACA CRC64;
MEYKSSGAIL AAEFSRRSLV KGGAICGLAA ASGALTLPFS RTAIAGAIAG EDAREKVVWS
ACTVNCGSRC PLRMHVVNDE IRYVETDNTG DDNYEGLHQV RACLRGRSMR RRVYNADRLK
YPMKRSGKRG EGKFERISWE EAFDTIASNM QRLIKDYGNE SIYLNYGTGT LGGTMTRSWP
PGNTLVARLM NCCGGYLNHY GDYSTAQIAE GLNYTYGGWA DGNSPSDIEN SRLVVLFGNN
PGETRMSGGG VTYYVEQARE RSDARMIIID PRYTDTGAGR EDEWIPIRPG TDAALVAALA
WVMINENLVD QPFLDKYCVG YDEKTLPAGA PANGHYKAYI LGQGSDGVAK TPAWASAITG
IPEARIIKLA REIATAKPAF ISQGWGPQRH ANGELVSRAI AMLPILTGNV GVHGGNSGAR
EGSYSLPFVR MPTLENPVQT SISMFLWTDA IERGPEMTAL KDGVRGKDKL DVPIKMVWNY
AGNCLVNQHS EINRTHEILQ DDQKCELIVV IDNHMTASAK YADILLPDCT ASEQMDFALD
ASCGNMAYVI FADQAIKPRF ECKTIYEMTS EIARRMGVEQ QFTEGRTQEE WLRHLYAQSR
EAIPELPDFD TFRRQGIFKK RDPEGHHVAY KAFRADPKAN PLTTPSGKIE IYSEQLAQIA
ASWQLQEDDV IDPLPVYSAG FENYDDPLSE KYPLQLTGFH YKARTHSTYG NVDVLKAACR
QEMWINPLDA RARGISNGER VRIFNGRGEV HIHAKVTPRI LPGVVALGEG AWYNPDANRI
DRAGSINVLT TQRPSPLAKG NPSHTNLVQV AKV
//
